SIR2B_DICDI
ID SIR2B_DICDI Reviewed; 778 AA.
AC Q54LF0;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=NAD-dependent deacetylase sir2B;
DE EC=2.3.1.286;
DE AltName: Full=Silent information regulator sir2B;
GN Name=sir2B; ORFNames=DDB_G0286671;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP DEVELOPMENTAL STAGE.
RX DOI=10.1264/jsme2.23.40;
RA Katayama T., Yasukawa H.;
RT "Developmental and spatial expression of sir2 genes in the cellular slime
RT mold Dictyostelium discoideum.";
RL Microbes Environ. 23:40-43(2008).
CC -!- FUNCTION: NAD-dependent deacetylase, which plays an important role in
CC the regulation of transcriptional repression. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in growing cells, but at
CC high levels in the prestalk-cell region during the developmental phase.
CC {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the sirtuin family. {ECO:0000305}.
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DR EMBL; AAFI02000089; EAL64091.1; -; Genomic_DNA.
DR RefSeq; XP_637611.1; XM_632519.1.
DR AlphaFoldDB; Q54LF0; -.
DR SMR; Q54LF0; -.
DR STRING; 44689.DDB0216432; -.
DR PaxDb; Q54LF0; -.
DR EnsemblProtists; EAL64091; EAL64091; DDB_G0286671.
DR GeneID; 8625751; -.
DR KEGG; ddi:DDB_G0286671; -.
DR dictyBase; DDB_G0286671; sir2B.
DR eggNOG; KOG2682; Eukaryota.
DR eggNOG; KOG4177; Eukaryota.
DR HOGENOM; CLU_359989_0_0_1; -.
DR InParanoid; Q54LF0; -.
DR OMA; IVHAHGS; -.
DR PRO; PR:Q54LF0; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 3.30.1600.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF02146; SIR2; 1.
DR SMART; SM00248; ANK; 10.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Metal-binding; NAD; Reference proteome; Repeat; Transferase;
KW Zinc.
FT CHAIN 1..778
FT /note="NAD-dependent deacetylase sir2B"
FT /id="PRO_0000393126"
FT REPEAT 83..112
FT /note="ANK 1"
FT REPEAT 114..142
FT /note="ANK 2"
FT REPEAT 148..178
FT /note="ANK 3"
FT REPEAT 191..221
FT /note="ANK 4"
FT REPEAT 225..255
FT /note="ANK 5"
FT REPEAT 260..289
FT /note="ANK 6"
FT REPEAT 317..354
FT /note="ANK 7"
FT REPEAT 358..390
FT /note="ANK 8"
FT REPEAT 394..423
FT /note="ANK 9"
FT DOMAIN 477..778
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 438..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 608
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 616
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 619
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 642
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 778 AA; 87973 MW; 75635CD0623B7507 CRC64;
MINILKDILY KSYSYLAFPF FYLGWAIKNS YQPNKTIKEE ESKPPKYPKE WSDLFIHSYN
NEHEKVLEII QKEPNSINSV DSLNWTPLHV AVSNKSIEVV TLLLERNIEI SIKRYTAFHI
AACNGDLNII EKMITMNRVP NGNILSNDME TSLFLSITNN HFEISEKIMD YYQSSMNSNE
FKKMIDQFNV HGVSPLIMSV LRKNLKMIKK LIEEGDADIN SFKKDNSTSL HCAAIIDFTE
AIEYLLDIGG IELMNSINRY GNSPIHEAAI KGNFKSIQTF INQLKKIIIK NNCSDGDSDK
DKLNLLLLEI IDKKDKDGST PLHLCCNCVN SDNIENNLKS CKVLIEEGGV QVNGIDSGNA
TALHILACVG EDKSLPLVKY FLSIGSDPTI ENKYGWTPIH QAYNNKNIQI YQLLLDHLKL
TNSTYKLDIE KKRVFQSSST STSSSSSSSS SSSSSSSSSS LLLNKEELKL KGIERLKNVI
NGIKKGEFKN VIVLSGAGIS ANAGIPPYRT KDGLLAKNKQ FSFSMEILEK HPDVFYQAIR
DHFYPIIKAS NDNDRDDGIS AGIKSTKSHY FINDLNEKYG CLLRNYTQNV DPLQERTGTP
TDKIIHAHGS FDQWYCTVCQ KQYTDKSDRI WREIGRGGLP FCTEPECRHV IRPNVVFFGE
PLSQDFRVNT ITDFRKADLL IVMGTSLIVY PFASLVNDVA SDVPRLLFNF ESTGPFVNTM
DLERKEKLKQ QQENESGESS NDNDNNELIV EARGNRDIVI LGDCDKGVDY FNTLFNSF
